The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Why does ribonuclease irreversibly inactivate at high temperatures?
Abstract
The mechanism of irreversible thermoinactivation of bovine pancreatic ribonuclease A in the pH range relevant to enzymatic catalysis has been elucidated. At 90 degrees C and pH 4, the enzyme inactivation is caused by hydrolysis of peptide bonds at aspartic acid residues (the main process) and deamidation of asparagine and/or glutamine residues. At 90 degrees C and neutral pH (pH 6 and 8), the enzyme inactivation is caused by a combination of disulfide interchange (the main process), beta-elimination of cystine residues, and deamidation of asparagine and/or glutamine residues. These four processes appear to demarcate the upper limit of thermostability of enzymes.
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Citations
Cites
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Stability of Proteins Small Globular Proteins
Privalov, P. L. (1979) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60460-x · Cited by 2,159
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Electrostatic Effects in Proteins
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Cited by
Stability of Protein Structure and Hydrophobic Interaction
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Stability of Protein Pharmaceuticals
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Enzymatic catalysis in nonaqueous solvents.
Zaks, A., & Klibanov, A. M. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69054-4 · Cited by 990
Self-citationEnzymatic catalysis in anhydrous organic solvents
Klibanov, A. (1989) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(89)90146-1 · Cited by 769
Self-citationNonenzymatic Deamidation of Asparaginyl and Glutaminyl Residues in Protein
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Metadata
- Authors
- Zale, S. E., & Klibanov, A. M.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1986-09-23
- Volume
- 25
- Issue
- 19
- Pages
- 5432-5444
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2004773817
- Cited by
- 275
- References
- 42
- FWCI
- 5.25
- Type
- journal article
- Language
- en
- Open access
- closed
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- Zale, S. E., & Klibanov, A. M. (1986). Why does ribonuclease irreversibly inactivate at high temperatures? Biochemistry. https://doi.org/10.1021/bi00367a014
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
